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Conserved domains on  [gi|974005168|ref|NP_001305689|]
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mitochondrial enolase superfamily member 1 isoform 4 [Homo sapiens]

Protein Classification

enolase-like domain-containing protein( domain architecture ID 1750080)

enolase-like domain-containing protein is an enzyme characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion

CATH:  3.20.20.120|3.30.390.10
Gene Ontology:  GO:0000287|GO:0003824
PubMed:  8987982|15581566

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
enolase_like super family cl40480
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ...
 1-238 0e+00

Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.


The actual alignment was detected with superfamily member cd03324:

Pssm-ID: 477366 [Multi-domain]  Cd Length: 415  Bit Score: 526.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   1 MLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAV 80
Cdd:cd03324  178 LLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAI 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  81 EWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSV 160
Cdd:cd03324  258 EWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAV 337

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974005168 161 LLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 238
Cdd:cd03324  338 LLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK 415
 
Name Accession Description Interval E-value
rTSbeta_L-fuconate_dehydratase cd03324
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ...
 1-238 0e+00

Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.


Pssm-ID: 239440 [Multi-domain]  Cd Length: 415  Bit Score: 526.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   1 MLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAV 80
Cdd:cd03324  178 LLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAI 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  81 EWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSV 160
Cdd:cd03324  258 EWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAV 337

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974005168 161 LLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 238
Cdd:cd03324  338 LLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK 415
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 23-241 1.96e-64

Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.


Pssm-ID: 463862 [Multi-domain]  Cd Length: 217  Bit Score: 200.48  E-value: 1.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   23 LKQLCAQALKD-GWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSP 100
Cdd:pfam13378   2 LAAEARRAVEArGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  101 DDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGL 180
Cdd:pfam13378  82 DDLEGLARLRRA---TPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPI 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974005168  181 cELVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 241
Cdd:pfam13378 159 -GLAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 4-245 1.64e-61

L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 443975 [Multi-domain]  Cd Length: 359  Bit Score: 197.35  E-value: 1.64e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   4 QGYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVE 81
Cdd:COG4948  125 DRVPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIR 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  82 WMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVL 161
Cdd:COG4948  201 LLRALEDLGLEWIEQPLPAEDLEGLAELRRA---TPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIA 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168 162 LMAKKFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVCEYVDHL---HEHFKYPVMIQRASYMPPKDPGYS 234
Cdd:COG4948  278 ALAEAHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIVELDGPLllaDDLVEDPLRIEDGYLTVPDGPGLG 348

                        250
                 ....*....|.
gi 974005168 235 TEMKEESVKKH 245
Cdd:COG4948  349 VELDEDALARY 359
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
 20-113 8.16e-30

Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.


Pssm-ID: 214914 [Multi-domain]  Cd Length: 97  Bit Score: 107.75  E-value: 8.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168    20 DDTLKQLCAQALKD-GWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 98
Cdd:smart00922   1 PEELAEAARRAVAEaGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80

                           90
                   ....*....|....*
gi 974005168    99 SPDDILGHATISKAL 113
Cdd:smart00922  81 PPDDLEGLAELRRAT 95
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
 46-178 1.48e-13

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 69.76  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  46 LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlVPLGIGIATGEQ 125
Cdd:PRK15440 191 LRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN-APAGMMVTSGEH 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 974005168 126 CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 178
Cdd:PRK15440 270 EATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSV 322
 
Name Accession Description Interval E-value
rTSbeta_L-fuconate_dehydratase cd03324
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ...
 1-238 0e+00

Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.


Pssm-ID: 239440 [Multi-domain]  Cd Length: 415  Bit Score: 526.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   1 MLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAV 80
Cdd:cd03324  178 LLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAI 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  81 EWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSV 160
Cdd:cd03324  258 EWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAV 337

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974005168 161 LLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 238
Cdd:cd03324  338 LLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK 415
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 23-241 1.96e-64

Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.


Pssm-ID: 463862 [Multi-domain]  Cd Length: 217  Bit Score: 200.48  E-value: 1.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   23 LKQLCAQALKD-GWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSP 100
Cdd:pfam13378   2 LAAEARRAVEArGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  101 DDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGL 180
Cdd:pfam13378  82 DDLEGLARLRRA---TPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPI 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974005168  181 cELVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 241
Cdd:pfam13378 159 -GLAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 4-245 1.64e-61

L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 443975 [Multi-domain]  Cd Length: 359  Bit Score: 197.35  E-value: 1.64e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   4 QGYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVE 81
Cdd:COG4948  125 DRVPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIR 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  82 WMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVL 161
Cdd:COG4948  201 LLRALEDLGLEWIEQPLPAEDLEGLAELRRA---TPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIA 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168 162 LMAKKFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVCEYVDHL---HEHFKYPVMIQRASYMPPKDPGYS 234
Cdd:COG4948  278 ALAEAHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIVELDGPLllaDDLVEDPLRIEDGYLTVPDGPGLG 348

                        250
                 ....*....|.
gi 974005168 235 TEMKEESVKKH 245
Cdd:COG4948  349 VELDEDALARY 359
MR_like cd03316
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ...
 7-236 1.76e-54

Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).


Pssm-ID: 239432 [Multi-domain]  Cd Length: 357  Bit Score: 179.34  E-value: 1.76e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   7 PAYTTSCAWlGYSDDTLKQLCAQALKDGWTRFKVKVGA------DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAV 80
Cdd:cd03316  128 RVYASGGGY-DDSPEELAEEAKRAVAEGFTAVKLKVGGpdsggeDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  81 EWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSV 160
Cdd:cd03316  207 RLARALEEYDLFWFEEPVPPDDLEGLARLRQA---TSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKI 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168 161 LLMAKKFEIPVCPHAGGVGLC-ELVQHLiifdyisvSASLEN-RVCEYVDHLHEH----FKYPVMIQRASYMPPKDPGYS 234
Cdd:cd03316  284 AALAEAHGVRVAPHGAGGPIGlAASLHL--------AAALPNfGILEYHLDDLPLredlFKNPPEIEDGYVTVPDRPGLG 355


                 ..
gi 974005168 235 TE 236
Cdd:cd03316  356 VE 357
MR_like_2 cd03327
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ...
 7-238 8.78e-32

Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.


Pssm-ID: 239443 [Multi-domain]  Cd Length: 341  Bit Score: 119.36  E-value: 8.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   7 PAYTTScawLGYSD-DTLKQLCAQALKDGWTRFKVKVG-------ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPE 78
Cdd:cd03327  110 PAYASG---LYPTDlDELPDEAKEYLKEGYRGMKMRFGygpsdghAGLRKNVELVRAIREAVGYDVDLMLDCYMSWNLNY 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  79 AVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENL 158
Cdd:cd03327  187 AIKMARALEKYELRWIEEPLIPDDIEGYAELKKA---TGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELK 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168 159 SVLLMAKKFEIPVCPHAGGVglceLVQHLIIFDYIS-VSASLEN-RVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTE 236
Cdd:cd03327  264 KIAALAEAYGVPVVPHASQI----YNYHFIMSEPNSpFAEYLPNsPDEVGNPLFYYIFLNEPVPVNGYFDLSDKPGFGLE 339


                 ..
gi 974005168 237 MK 238
Cdd:cd03327  340 LN 341
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
 20-113 8.16e-30

Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.


Pssm-ID: 214914 [Multi-domain]  Cd Length: 97  Bit Score: 107.75  E-value: 8.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168    20 DDTLKQLCAQALKD-GWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 98
Cdd:smart00922   1 PEELAEAARRAVAEaGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80

                           90
                   ....*....|....*
gi 974005168    99 SPDDILGHATISKAL 113
Cdd:smart00922  81 PPDDLEGLAELRRAT 95
enolase_like cd00308
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ...
 26-187 1.73e-27

Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.


Pssm-ID: 238188 [Multi-domain]  Cd Length: 229  Bit Score: 105.49  E-value: 1.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  26 LCAQALK-------DGWTRFKVKVGADLqddmRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 98
Cdd:cd00308   54 LAAKALGvplaellGGGSRDRVPAYGSI----ERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPC 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  99 SPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 178
Cdd:cd00308  130 APDDLEGYAALRRR---TGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLE 206

                        170
                 ....*....|.
gi 974005168 179 G--LCELVQHL 187
Cdd:cd00308  207 SsiGTAAALHL 217
MR_like_3 cd03328
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ...
 7-174 2.91e-25

Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.


Pssm-ID: 239444 [Multi-domain]  Cd Length: 352  Bit Score: 102.11  E-value: 2.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   7 PAYTtSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKL 86
Cdd:cd03328  127 PVYG-SGGFTSYDDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAF 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  87 AKFKPLWIEEPTSPDDILGHATIsKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKK 166
Cdd:cd03328  206 ADEGVTWFEEPVSSDDLAGLRLV-RERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAA 284


                 ....*...
gi 974005168 167 FEIPVCPH 174
Cdd:cd03328  285 HHVDLSAH 292
mandelate_racemase cd03321
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ...
 29-246 5.30e-18

Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.


Pssm-ID: 239437 [Multi-domain]  Cd Length: 355  Bit Score: 82.15  E-value: 5.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  29 QALKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHA 107
Cdd:cd03321  151 TAAEEGFHAVKTKIGyPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHA 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168 108 TISKAL-VPLGIgiatGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHaggvglcelvqh 186
Cdd:cd03321  231 RIASALrTPVQM----GENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH------------ 294

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974005168 187 liIFDYISV---SASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQ 246
Cdd:cd03321  295 --LFQEISAhllAVTPTAHWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKYL 355
MLE_like cd03315
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ...
 29-187 2.08e-16

Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and residues that can function as general acid/base catalysts, a Lys-X-Lys motif and another conserved lysine. Despite these conserved residues, the members of the MLE subgroup, like muconate lactonizing enzyme, o-succinylbenzoate synthase (OSBS) and N-acylamino acid racemase (NAAAR), catalyze different reactions.


Pssm-ID: 239431 [Multi-domain]  Cd Length: 265  Bit Score: 76.61  E-value: 2.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  29 QALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHAT 108
Cdd:cd03315   95 RALEAGFRTFKLKVGRDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAA 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168 109 ISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPV---CPHAGGVGLCELVq 185
Cdd:cd03315  175 LARA---TDTPIMADESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVmvgSMIESGLGTLANA- 250


                 ..
gi 974005168 186 HL 187
Cdd:cd03315  251 HL 252
OSBS cd03320
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ...
 11-171 8.75e-16

o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate (o-succinylbenzoate or OSB), a reaction in the menaquinone biosynthetic pathway. Menaquinone is an essential cofactor for anaerobic growth in eubacteria and some archaea. OSBS belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.


Pssm-ID: 239436 [Multi-domain]  Cd Length: 263  Bit Score: 74.60  E-value: 8.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  11 TSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKF 89
Cdd:cd03320   74 PVNALLPAGDAAALGEAKAAYGGGYRTVKLKVGAtSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  90 KPLWIEEPTSPDDILGHatisKALVpLGIGIATGEqchnrvifkQLLQAKALQFLQIDSC---------RLGSVNENLSV 160
Cdd:cd03320  154 RIEYIEQPLPPDDLAEL----RRLA-AGVPIALDE---------SLRRLDDPLALAAAGAlgalvlkpaLLGGPRALLEL 219

                        170
                 ....*....|.
gi 974005168 161 LLMAKKFEIPV 171
Cdd:cd03320  220 AEEARARGIPA 230
D-galactonate_dehydratase cd03325
D-galactonate dehydratase catalyses the dehydration of galactonate to ...
 14-180 1.20e-14

D-galactonate dehydratase catalyses the dehydration of galactonate to 2-keto-3-deoxygalactonate (KDGal), as part of the D-galactonate nonphosphorolytic catabolic Entner-Doudoroff pathway. D-galactonate dehydratase belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.


Pssm-ID: 239441 [Multi-domain]  Cd Length: 352  Bit Score: 72.36  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  14 AWLG-YSDDTLKQLCAQALKDGWTRFK---------VKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWM 83
Cdd:cd03325  117 SWIGgDRPSDVAEAARARREAGFTAVKmnateelqwIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLA 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  84 SKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLM 163
Cdd:cd03325  197 KELEPYRLLFIEEPVLPENVEALAEIAAR---TTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAM 273

                        170
                 ....*....|....*....
gi 974005168 164 AKKFEIPVCPHA--GGVGL 180
Cdd:cd03325  274 AEAYDVALAPHCplGPIAL 292
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
 46-178 1.48e-13

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 69.76  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  46 LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlVPLGIGIATGEQ 125
Cdd:PRK15440 191 LRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN-APAGMMVTSGEH 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 974005168 126 CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 178
Cdd:PRK15440 270 EATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSV 322
MR_like_1 cd03326
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ...
 34-124 1.86e-12

Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.


Pssm-ID: 239442 [Multi-domain]  Cd Length: 385  Bit Score: 66.26  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  34 GWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKA 112
Cdd:cd03326  175 GYTVVKIKIGgAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADH 254

                         90
                 ....*....|..
gi 974005168 113 LVPlgiGIATGE 124
Cdd:cd03326  255 YDG---PIATGE 263
PRK14017 PRK14017
galactonate dehydratase; Provisional
 28-244 8.84e-12

galactonate dehydratase; Provisional


Pssm-ID: 184455 [Multi-domain]  Cd Length: 382  Bit Score: 64.15  E-value: 8.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  28 AQALKD-GWTRFKVKVGADLQ--DDMR-------RCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEP 97
Cdd:PRK14017 132 ARARVErGFTAVKMNGTEELQyiDSPRkvdaavaRVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEP 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  98 TSPD------DILGHATISkalvplgigIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPV 171
Cdd:PRK14017 212 VLPEnaealpEIAAQTSIP---------IATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVAL 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168 172 CPHA--GGVGLCELVQhliiFDYISVSASLE--------NRVCEYVDHL--HEHFKYpvmiqRASYM-PPKDPGYSTEMK 238
Cdd:PRK14017 283 APHCplGPIALAACLQ----VDAVSPNAFIQeqslgihyNQGADLLDYVknKEVFAY-----EDGFVaIPTGPGLGIEID 353


                 ....*.
gi 974005168 239 EESVKK 244
Cdd:PRK14017 354 EAKVRE 359
L-Ala-DL-Glu_epimerase cd03319
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The ...
 28-129 1.22e-11

L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.


Pssm-ID: 239435 [Multi-domain]  Cd Length: 316  Bit Score: 63.36  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  28 AQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIgPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHA 107
Cdd:cd03319  143 KKAAKRGFPLLKIKLGGDLEDDIERIRAIREAA-PDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLA 221

                         90       100
                 ....*....|....*....|..
gi 974005168 108 TISKAlvpLGIGIATGEQCHNR 129
Cdd:cd03319  222 YLRDK---SPLPIMADESCFSA 240
MLE cd03318
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ...
 37-116 3.74e-11

Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.


Pssm-ID: 239434 [Multi-domain]  Cd Length: 365  Bit Score: 62.33  E-value: 3.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  37 RFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATI-SKALV 114
Cdd:cd03318  161 RFKLKMGArPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLrSRNRV 240


                 ..
gi 974005168 115 PL 116
Cdd:cd03318  241 PI 242
PRK02901 PRK02901
O-succinylbenzoate synthase; Provisional
 34-97 1.48e-08

O-succinylbenzoate synthase; Provisional


Pssm-ID: 235084 [Multi-domain]  Cd Length: 327  Bit Score: 54.59  E-value: 1.48e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974005168  34 GWTRFKVKV---GADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPL-WIEEP 97
Cdd:PRK02901 102 GCRTAKVKVaepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALDADGPLeYVEQP 169
RspA cd03322
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ...
 52-254 1.53e-07

The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose putative targets are homoserine lactone (HSL)-derivative. They are part of the mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subfamily share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and catalytic residues, a partially conserved Lys-X-Lys motif and a conserved histidine-aspartate dyad.


Pssm-ID: 239438 [Multi-domain]  Cd Length: 361  Bit Score: 51.67  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  52 RCQI------IRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATI-SKALVPlgigIATGE 124
Cdd:cd03322  146 RVQLpklfeaVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIrQHTATP----LAVGE 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168 125 QCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEI-----------PVCpHAGGVGLCELVQHLIIFDYI 193
Cdd:cd03322  222 VFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVrtgwhgptdlsPVG-MAAALHLDLWVPNFGIQEYM 300

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974005168 194 SvsaslenrvceYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQY----------PDGEVWK 254
Cdd:cd03322  301 R-----------HAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYvprylpvarlEDGTVHN 360
NAAAR cd03317
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ...
 20-244 3.14e-07

N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of N-acylamino acids. NAAARs act on a broad range of N-acylamino acids rather than amino acids. Enantiopure amino acids are of industrial interest as chiral building blocks for antibiotics, herbicides, and drugs. NAAAR is a member of the enolase superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.


Pssm-ID: 239433 [Multi-domain]  Cd Length: 354  Bit Score: 50.70  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  20 DDTLKQLcAQALKDGWTRFKVKVGAdlQDDMRRCQIIRDMIgPEKTLMMDAN---QRWDVPEavewMSKLAKFKPLWIEE 96
Cdd:cd03317  139 EQLLKQI-ERYLEEGYKRIKLKIKP--GWDVEPLKAVRERF-PDIPLMADANsayTLADIPL----LKRLDEYGLLMIEQ 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  97 PTSPDDILGHATISKAL---VPLGIGIATGEQChnrvifKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCp 173
Cdd:cd03317  211 PLAADDLIDHAELQKLLktpICLDESIQSAEDA------RKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVW- 283

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974005168 174 HAG----GVGLCELVQ--HLIIFDY-ISVSASleNRvceyvdHLHEHF-KYPVMIQRASYMPPKDPGYSTEMKEESVKK 244
Cdd:cd03317  284 CGGmlesGIGRAHNVAlaSLPNFTYpGDISAS--SR------YFEEDIiTPPFELENGIISVPTGPGIGVTVDREALKK 354
MR_like_4 cd03329
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ...
 7-178 7.28e-07

Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.


Pssm-ID: 239445 [Multi-domain]  Cd Length: 368  Bit Score: 49.70  E-value: 7.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   7 PAY-TTSCAWLGYSDDTLKQLC--AQALKD-GWTRFKVK--VGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAV 80
Cdd:cd03329  127 PAYaSTMVGDDLEGLESPEAYAdfAEECKAlGYRAIKLHpwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADAL 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  81 EWMSKLAKFKPLWIEEPTSPDDILGHATISKAL-VPLGIGIATGEQCHNRVIFkqlLQAKALQFLQIDSCRLGSVNENLS 159
Cdd:cd03329  207 RLGRALEELGFFWYEDPLREASISSYRWLAEKLdIPILGTEHSRGALESRADW---VLAGATDFLRADVNLVGGITGAMK 283

                        170
                 ....*....|....*....
gi 974005168 160 VLLMAKKFEIPVCPHAGGV 178
Cdd:cd03329  284 TAHLAEAFGLDVELHGNGA 302
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 26-104 1.16e-06

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 49.47  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168   26 LCAQALKDGWTRFKVKVG--ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEP-TSPDD 102
Cdd:PLN02980 1097 VARKLVEEGFSAIKLKVGrrVSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPvQDEDD 1176


                  ..
gi 974005168  103 IL 104
Cdd:PLN02980 1177 LI 1178
PRK02714 PRK02714
o-succinylbenzoate synthase;
10-101 1.30e-04

o-succinylbenzoate synthase;


Pssm-ID: 235061 [Multi-domain]  Cd Length: 320  Bit Score: 42.69  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005168  10 TTSCAWLGYSDDTLKQLcAQALKDGWTRFKVKVGAD-LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 88
Cdd:PRK02714 110 LSYSALLPAGEAALQQW-QTLWQQGYRTFKWKIGVDpLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAKRWLQLCDR 188

                         90
                 ....*....|....*.
gi 974005168  89 FKPL---WIEEPTSPD 101
Cdd:PRK02714 189 RLSGkieFIEQPLPPD 204
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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